Klein Taq is a derivative of Taq DNA polymerase. It is a 5'-exo-minus N-terminally truncated Thermus aquaticus DNA polymerase. Expressed from a gene construct in E. coli, translation initiates at Met236, bypassing the 5'-3' exonuclease domain of the DNA polymerase-encoding gene. The enzyme reveals a highly active and even more heat-stable DNA polymerase activity in comparison with Taq DNA polymerase. The optimal range of the Mg2+ concentration for Klein Taq is broader than that for the majority of thermostable polymerases. This feature permits to optimize reaction conditions easier than for other polymerases. Repeated exposure to 98 C does not diminish the enzyme activity. Significant activity remains even after exposure to 99 C.

The mutation rate during polymerization is twofold lower for Klein Taq as compared to the full-length Taq DNA polymerase. Klein Taq has a very low 'background' ability to extend a mismatched 3'-oligonucleotide end making it suitable for mutation analysis with mutation-specific oligonucleotides.

* The product is tested for the absence of endonucleases/ nickases and exonucleases.

*Unit definition: One unit of activity is defined as the amount of enzyme required to incorporate 10 nmoles of dNTP into acid-insoluble DNA fraction in 30 minutes at 72 C.

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